Abz-FRK(Dnp)P-OH trifluoroacetate (TFA) is a substrate for the Angiotensin Converting Enzyme (ACE). Abz-FRK(Dnp)P-OH TFA has been used to study both the reduction of mortality of patients with sepsis and paracetamol-induced hypothermia.
Biochem/physiol Actions
Substrate for ACE (Angiotensin Converting Enzyme). Internally quenched fluorogenic substrate for Real Time Fluorescent Assay.
Features and Benefits
This compound is featured on the Angiotensin Receptors page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.
British journal of pharmacology, 173(8), 1314-1328 (2016-03-31)
Using an in-house bioinformatics programme, we identified and synthesized a novel nonapeptide, H-Pro-Pro-Thr-Thr-Thr-Lys-Phe-Ala-Ala-OH. Here, we have studied its biological activity, in vitro and in vivo, and have identified its target in the brain. The affinity of the peptide was characterized
Journal of veterinary science, 12(1), 21-25 (2011-03-04)
Angiotensin-I converting enzyme (ACE) is a key regulator of blood pressure, electrolytes and fluid homeostasis through conversion of angiotensin I into angiotensin II. Recently, a genetic polymorphism of the ACE gene, which accounts for 47% of the variation of ACE
The local administration of μ-opioid receptor (MOR) agonists attenuates neuropathic pain but the precise mechanism implicated in this effect is not completely elucidated. We investigated if nitric oxide synthesized by neuronal (NOS1) or inducible (NOS2) nitric oxide synthases could modulate
Drug metabolism and disposition: the biological fate of chemicals, 39(9), 1689-1695 (2011-06-02)
In recent years, there has been increasing interest in hypothermia induced by paracetamol for therapeutic purposes, which, in some instances, has been reported as a side effect. Understanding the mechanism by which paracetamol induces hypothermia is therefore an important question.
Quenched fluorescence peptides were used to investigate the substrate specificity requirements for recombinant wild-type angiotensin I-converting enzyme (ACE) and two full-length mutants bearing a single functional active site (N- or C-domain). We assayed two series of bradykinin-related peptides flanked by
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